[期刊论文][research article]


Glycine Perturbs Local and Global Conformational Flexibility of a Transmembrane Helix

作   者:
Alexander Go?tz;Maximilian Ebert;Walter Stelzer;Christina Scharnagl;Philipp Ho?gel;Felix Kuhne;Kasper D. Rand;Dieter Langosch;

出版年:2018

页     码:1326 - 1337
出版社:American Chemical Society


摘   要:

Flexibletransmembrane helices frequently support the conformationaltransitions between different functional states of membrane proteins.While proline is well known to distort and destabilize transmembranehelices, the role of glycine is still debated. Here, we systematicallyinvestigated the effect of glycine on transmembrane helix flexibilityby placing it at different sites within the otherwise uniform leucine/valinerepeat sequence of the LV16 model helix. We show that amide deuterium/hydrogenexchange kinetics are increased near glycine. Molecular dynamics simulationsreproduce the measured exchange kinetics and reveal, at atomic resolution,a severe packing defect at glycine that enhances local hydration.Furthermore, glycine alters H-bond occupancies and triggers a redistributionof α-helical and 310-helical H-bonds. These effectsfacilitate local helix bending at the glycine site and change thecollective dynamics of the helix.



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所属期刊
Biochemistry
ISSN: 0006-2960
来自:American Chemical Society